Interaction of peptide backbones and transition metal ions: 1. an IM-MS and DFT study of the binding pattern, structure and fragmentation of Pd(II)/Ni(II)-Polyalanine complexes

Liu, Ziye; Chen, Siyun; Qiao, Fangfang; Zhang, Xinhao

doi:10.1016/j.ijms.2018.12.016

Cited by 10 publications

(4 citation statements)

References 76 publications

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“…Metal ions have been extensively studied for their interactions with important biomolecules such as amino acids [ 10 , 11 ], peptides [ 12 , 13 ], and proteins [ 14 , 15 ], which are involved in structural functions, cell signaling, cell expression, and hormone synthesis, to name a few [ 16 , 17 ]. Proteins often need to interact with metal ions to carry out their function [ 18 ].…”

Section: Introductionmentioning

confidence: 99%

Bioinorganic Chemistry of Micronutrients Related to Alzheimer’s and Parkinson’s Diseases

Kola,

Nencioni,

Valensin

2023

Molecules

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Metal ions are fundamental to guarantee the regular physiological activity of the human organism. Similarly, vitamins play a key role in many biological functions of the metabolism, among which are coenzymes, redox mediators, and antioxidants. Due to their importance in the human organism, both metals and vitamins have been extensively studied for their involvement in neurodegenerative diseases (NDs). However, the full potential of the interaction between vitamins and metal ions has not been fully explored by researchers yet, and further investigation on this topic is needed. The aim of this review is to provide an overview of the scientific literature on the implications of vitamins and selected metal ions in two of the most common neurodegenerative diseases, Alzheimer’s and Parkinson’s disease. Furthermore, vitamin–metal ion interactions are discussed in detail focusing on their bioinorganic chemistry, with the perspective of arousing more interest in this fascinating bioinorganic field.

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Section: Introductionmentioning

confidence: 99%

Bioinorganic Chemistry of Micronutrients Related to Alzheimer’s and Parkinson’s Diseases

Kola,

Nencioni,

Valensin

2023

Molecules

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“…The characterization at the molecular level is typically performed by several techniques: 2D NMR, circular dichroism, and X-ray diffraction for probing peptide helicity; FRET for identifying the analyte binding and for estimating the structural changes in the recipient; molecular dynamic and DFT calculations for predicting the binding site, to be compared with experimental data; microscopies for characterizing peptide supramolecular organizations, fluorescence spectroscopy for studying peptide-ion binding and revealing the complex structure, isothermal titration calorimetry, mass spectrometry, as well as other methods [7,19,22,24,[30][31][32][33][34][35].…”

Section: Introductionmentioning

confidence: 99%

A Peptide-Based Trap for Metal Ions Studied by Electron Paramagnetic Resonance

et al. 2022

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Peptide-based materials provide a versatile platform for sensing and ion sequestration since peptides are endowed with stimuli-responsive properties. The mechanism of molecular sensing is often based on peptide structural changes (or switching), caused by the binding of the target molecule. One scope of sensing applications is the selection of a specific analyte, which may be achieved by adjusting the structure of the peptide binding site. Therefore, exact knowledge of peptide properties and 3D-structure in the ‘switched’ state is desirable for tuning the detection and for further molecular construction. Hence, here we demonstrate the performance of Electron Paramagnetic Resonance (EPR) spectroscopy in the identification of metal ion binding by the antimicrobial peptide trichogin GA IV. Na(I), Ca(II), and Cu(II) ions were probed as analytes to evaluate the impact of coordination number, ionic radii, and charge. Conclusions drawn by EPR are in line with literature data, where other spectroscopic techniques were exploited to study peptide-ion interactions for trichogin GA IV, and the structural switch from an extended helix to a hairpin structure, wrapped around the metal ion upon binding of divalent cations was proposed.

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“…5 The wound healing and antiaging properties of GHK are due probably to its strong affinity for copper ions (Cu 2+ ) to form GHK-Cu complexes. [6][7][8][9][10] Except for formation of the GHK-Cu complexes, protonation is also favored for GHK since the proton affinity of the His side chain is high. [11][12][13] Experimentally and theoretically, there is compelling evidence for formation of nondirectly sequential ions via cyclization/reopening chemistry in the collisioninduced dissociation (CID) spectra of the b n ions when the His residue is near the C-terminus of peptides.…”

Section: Introductionmentioning

confidence: 99%

Mass spectral and theoretical investigations of the transient proton-bound dimers on the cleavage processes of the peptide GHK and its analogues

Wang

Zhang

et al. 2021

RSC Adv.

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Interaction of peptide backbones and transition metal ions: 1. an IM-MS and DFT study of the binding pattern, structure and fragmentation of Pd(II)/Ni(II)-Polyalanine complexes

Cited by 10 publications

References 76 publications

Bioinorganic Chemistry of Micronutrients Related to Alzheimer’s and Parkinson’s Diseases

Bioinorganic Chemistry of Micronutrients Related to Alzheimer’s and Parkinson’s Diseases

A Peptide-Based Trap for Metal Ions Studied by Electron Paramagnetic Resonance

Mass spectral and theoretical investigations of the transient proton-bound dimers on the cleavage processes of the peptide GHK and its analogues

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